Details
Structure visualisation
Entry information
| Complex | |
| AACDB_ID: | 1015 |
| PDBID: | 4W6X |
| Chains: | B_A |
| Organism: | Escherichia coli, Lama glama |
| Method: | XRD |
| Resolution (Å): | 1.88 |
| Reference: | 10.1371/journal.pone.0114691 |
| Antibody | |
| Antibody: | NbFedF7 Nanobody |
| Antibody mutation: | No |
| INN (Clinical Trial): | |
| Antigen | |
| Antigen: | F18 fimbrial adhesin AC |
| Antigen mutation: | No |
| Durg Target: | |
Sequence information
Antibody
Chain: B
Mutation: NULL
| >4W6X_B|Chain B|Nanobody NbFedF7|Lama glama (9844) QVQLQESGGGSVQAGGSLRLSCTASGYTYRKYCMGWFRQAPGKEREGVACINSGGGTSYYADSVKGRFTISQDNAKDTVFLRMNSLKPEDTAIYYCALSSNSVCPPGHVAWYNDWGQGTQVTVSSHHHHHH |
Antigen
Chain: A
Mutation: NULL
| >4W6X_A|Chain A|F18 fimbrial adhesin AC|Escherichia coli (562) NSSASSAQVTGTLLGTGKTNTTQMPALYTWQHQIYNVNFIPSSSGTLTCQAGTILVWKNGRETQYALECRVSIHHSSGSINESQWGQQSQVGFGTACGNKKCRFTGFEISLRIPPNAQTYPLSSGDLKGSFSLTNKEVNWSASIYVPAIAK |
Interaction
1、Solvent accessible surface areas (SASA) were calculated (Naccess V2.1.1) for each residue in antibody and antigen, respectively. The residues with SASA loss in binding of more than 1Å2 were classified as interacting residues.
Interacting residues (ΔSASA based)
| B: TYR29 ARG30 LYS31 ARG45 SER100 ASN101 SER102 VAL103 PRO105 PRO106 HIS108 VAL109 ALA110 TRP111 TYR112 ASN113 ASP114 TRP115 A: SER58 GLY59 THR60 ILE87 HIS89 SER91 SER93 ILE94 ASN95 GLU96 SER97 GLN98 GLN102 SER103 GLN104 VAL105 GLY106 PHE107 GLY108 ALA110 CYS111 GLY112 CYS116 PHE118 |
2、We defined interacting paratope-epitope residues by a distance cutoff of < 5Å . Two amino acids are considered as interacting residues if they have at least one atom within a distance of 5 Å from any atom.
Interacting residues (Atom distance based)
